Effects of drug-binding on the thermal denaturation of human serum albumin

Asymmetric thermograms of defatted albumin, alone and in the presence of two model drugs, have been obtained in phosphate buffers at three pH values. The albumin is less thermally stable in the N form, but is protected by both drugs. The nonsteroidal antiinflammatory benoxaprofen offers more protect...

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Bibliographic Details
Published inJournal of pharmaceutical and biomedical analysis Vol. 12; no. 12; p. 1501
Main Authors Lohner, K, Sen, A C, Prankerd, R, Esser, A F, Perrin, J H
Format Journal Article
LanguageEnglish
Published England 01.12.1994
Subjects
Anti-Inflammatory Agents, Non-Steroidal - pharmacology
Binding Sites
Calorimetry, Differential Scanning
Humans
Propionates - pharmacology
Protein Denaturation
Serum Albumin - chemistry
Warfarin - pharmacology
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Summary:Asymmetric thermograms of defatted albumin, alone and in the presence of two model drugs, have been obtained in phosphate buffers at three pH values. The albumin is less thermally stable in the N form, but is protected by both drugs. The nonsteroidal antiinflammatory benoxaprofen offers more protection than warfarin against thermal denaturation.
ISSN:0731-7085
DOI:10.1016/0731-7085(94)00094-8